PMID- 24409183 OWN - NLM STAT- PubMed-not-MEDLINE DCOM- 20140624 LR - 20220311 IS - 1664-3224 (Print) IS - 1664-3224 (Electronic) IS - 1664-3224 (Linking) VI - 4 DP - 2013 Dec 27 TI - Dendritic cells: a spot on sialic Acid. PG - 491 LID - 10.3389/fimmu.2013.00491 [doi] LID - 491 AB - Glycans decorating cell surface and secreted proteins and lipids occupy the juncture where critical host-host and host-pathogen interactions occur. The role of glycan epitopes in cell-cell and cell-pathogen adhesive events is already well-established, and cell surface glycan structures change rapidly in response to stimulus and inflammatory cues. Despite the wide acceptance that glycans are centrally implicated in immunity, exactly how glycans and their changes contribute to the overall immune response remains poorly defined. Sialic acids are unique sugars that usually occupy the terminal position of the glycan chains and may be modified by external factors, such as pathogens, or upon specific physiological cellular events. At cell surface, sialic acid-modified structures form the key fundamental determinants for a number of receptors with known involvement in cellular adhesiveness and cell trafficking, such as the Selectins and the Siglec families of carbohydrate recognizing receptors. Dendritic cells (DCs) preside over the transition from innate to the adaptive immune repertoires, and no other cell has such relevant role in antigen screening, uptake, and its presentation to lymphocytes, ultimately triggering the adaptive immune response. Interestingly, sialic acid-modified structures are involved in all DC functions, such as antigen uptake, DC migration, and capacity to prime T cell responses. Sialic acid content changes along DC differentiation and activation and, while, not yet fully understood, these changes have important implications in DC functions. This review focuses on the developmental regulation of DC surface sialic acids and how manipulation of DC surface sialic acids can affect immune-critical DC functions by altering antigen endocytosis, pathogen and tumor cell recognition, cell recruitment, and capacity for T cell priming. The existing evidence points to a potential of DC surface sialylation as a therapeutic target to improve and diversify DC-based therapies. FAU - Crespo, Helio J AU - Crespo HJ AD - CEDOC - UC Imunologia, Faculdade de Ciencias Medicas, Universidade Nova de Lisboa , Lisbon , Portugal ; Department of Molecular and Cellular Biology, Roswell Park Cancer Institute , Buffalo, NY , USA. FAU - Lau, Joseph T Y AU - Lau JT AD - Department of Molecular and Cellular Biology, Roswell Park Cancer Institute , Buffalo, NY , USA. FAU - Videira, Paula A AU - Videira PA AD - CEDOC - UC Imunologia, Faculdade de Ciencias Medicas, Universidade Nova de Lisboa , Lisbon , Portugal. LA - eng GR - P01 HL107146/HL/NHLBI NIH HHS/United States GR - R01 AI056082/AI/NIAID NIH HHS/United States PT - Journal Article PT - Review DEP - 20131227 PL - Switzerland TA - Front Immunol JT - Frontiers in immunology JID - 101560960 PMC - PMC3873530 OTO - NOTNLM OT - dendritic cell OT - host-pathogen interaction OT - lectins OT - sialic acid OT - sialylation EDAT- 2014/01/11 06:00 MHDA- 2014/01/11 06:01 PMCR- 2013/01/01 CRDT- 2014/01/11 06:00 PHST- 2013/09/30 00:00 [received] PHST- 2013/12/15 00:00 [accepted] PHST- 2014/01/11 06:00 [entrez] PHST- 2014/01/11 06:00 [pubmed] PHST- 2014/01/11 06:01 [medline] PHST- 2013/01/01 00:00 [pmc-release] AID - 10.3389/fimmu.2013.00491 [doi] PST - epublish SO - Front Immunol. 2013 Dec 27;4:491. doi: 10.3389/fimmu.2013.00491.